ID A0A2N6P0G1_BEABA Unreviewed; 186 AA.
AC A0A2N6P0G1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Guanine nucleotide-binding protein alpha-1 subunit {ECO:0000313|EMBL:PMB73002.1};
GN Name=gna-1 {ECO:0000313|EMBL:PMB73002.1};
GN ORFNames=BM221_000419 {ECO:0000313|EMBL:PMB73002.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB73002.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB73002.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB73002.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC {ECO:0000256|ARBA:ARBA00011356}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000256|ARBA:ARBA00007976}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PMB73002.1}.
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DR EMBL; MRVG01000001; PMB73002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6P0G1; -.
DR OMA; RICEKDY; -.
DR Proteomes; UP000235728; Unassembled WGS sequence.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR002975; Fungi_Gprotein_alpha.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10218:SF355; GUANINE NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR01241; GPROTEINAFNG.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000235728}.
SQ SEQUENCE 186 AA; 21710 MW; A6656E616147A158 CRC64;
MPNDQDVLRS RVKTTGITET TFIIGDLTYR MFDVGGQRSE RKKWIHCFEN VTTILFLVAI
SEYDQLLFED ETVNRMQEAL TLFDSICNSR WFTKTSIILF LNKIDRFKEK LPVSPMKNYF
PDYEGGDDYA AACDYILNRF VSLNQHENKQ IYTHFTCATD TTQIRFVMAA VNDIIIQENL
RLCGLI
//
